Screening for nitric oxide-dependent protein-protein interactions.

Journal Article (Journal Article)

Because nitric oxide (NO) may be a ubiquitous regulator of cellular signaling, we have modified the yeast two-hybrid system to explore the possibility of NO-dependent protein-protein interactions. We screened for binding partners of procaspase-3, a protein implicated in apoptotic signaling pathways, and identified multiple NO-dependent interactions.Two such interactions, with acid sphingomyelinase and NO synthase, were shown to occur in mammalian cells dependent on endogenous NO. Nitrosylation may thus provide a broad-based mechanism for regulating interactions between proteins. If so, systematic proteomic analyses in which redox state and NO bioavailability are carefully controlled will reveal a large array of novel interactions.

Full Text

Duke Authors

Cited Authors

  • Matsumoto, A; Comatas, KE; Liu, L; Stamler, JS

Published Date

  • August 1, 2003

Published In

Volume / Issue

  • 301 / 5633

Start / End Page

  • 657 - 661

PubMed ID

  • 12893946

Pubmed Central ID

  • 12893946

Electronic International Standard Serial Number (EISSN)

  • 1095-9203

Digital Object Identifier (DOI)

  • 10.1126/science.1079319


  • eng

Conference Location

  • United States